Studies of the release and turnover of a human neutrophil lipocalin

L. Axelsson, M. Bergenfeldt, K. Ohlsson

Research output: Contribution to journalArticlepeer-review

Abstract

A 24-kDa protein was purified from human neutrophil extracts and shown to be the newly discovered neutrophil gelatinase-associated lipocalin (NGAL), based on structural and immunochemical data. A specific enzyme-linked immunosorbent assay (ELISA) was developed for the determination of NGAL in human plasma and tissue fluids. Normal human plasma contains 72 μg 1-1 of NGAL (range 40-109 μg 1-1) in two main forms, monomer and dimer. 35S-methionine metabolic studies of human neutrophils showed that granulocyte macrophagecolony-stimulating factor (GMCSF) stimulated significant synthesis and secretion of NGAL in a dose- and time-dependent fashion. NGAL was rapidly released as monomer and dimer on incubation of heparinized whole blood with opsonized yeast, reaching a plateau corresponding to about 35% of total cell content after 30 min. Following intravenous injection of 125-iodine labelled NGAL there was a more rapid initial clearance of the monomeric than of the dimeric form; t1/2 10 min vs. 20 min. During the second phase the two forms cleared at similar rates. Severe acute peritonitis was accompanied by a 10-fold increase in NGAL plasma levels and the NGAL level in peritoneal exudates, which reached about 40 mg 1-1. There was a good linear correlation between the concentrations of NGAL, leucocyte elastase and NP4 (neutrophil proteinase 4 = P3).

Original languageEnglish
Pages (from-to)577-588
Number of pages12
JournalScandinavian Journal of Clinical and Laboratory Investigation
Volume55
Issue number7
DOIs
Publication statusPublished - 1995

Subject classification (UKÄ)

  • Medicinal Chemistry

Keywords

  • Cytokines
  • ELISA
  • Leucocyte proteinases
  • Lipocalin
  • Neutrophil
  • Peritonitis
  • Phagocytosis

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